Corynebacterium, especially Corynebacterium glutamicum is gram positive microorganism which have been largely used for producing L-amino acid. L-amino acid, especially L-lysine is mainly produced by the fermentation with Corynebacterium strain, which is used in an animal feed and human medicine and cosmetics industries.
On this wise, a diversity of attempt have been performed to improve a production method of L-amino acid using Corynebacterium glutamicum since it holds an important position in industries.
Particularly, there have been many researches that each of genes relating to L-amino acid biosynthesis is amplified by the DNA recombination technique to examine effects on the formation of L-amino acid and thus to improve Corynebacterium strain for producing L-amino acid [Kinoshita, “glutamic acid bacteria” in Biology of industrial Microorganisms, Demain and Solomon (Eds), Benjamin Chummings, London, UK, 1985, 115-142; Hilinger, BioTec 2, 40-44 (1991); Eggeling, Amino Acids 6, 261-272 (1994); Jetten and Sinskey, Critical Reviews in Biotechnology 15, 73-103 (1995); and Sahm et al., Annuals of the New York Academy of Acience 782, 25-39 (1996)].
In addition, research have been performed by the destruction or the underexpression of a specific gene to improve Corynebacterium strain which produces L-amino acid. For example, the Korean Published Patent Application Nos. 2001-51915 and 2001-62279 in the name of Degusa-Huels Acktiengeselshaft disclosed method for enhancing the productivity of L-amino acid from Corynebacterium by the under-expression of sucC and sucD gene and zwa2 gene derived from Corynebacterium glutamicum. 
In addition, it is disclosed a method for introducing gene from other bacteria in the outside. For example, the Japanese Patent No. H07-121228 disclosed method for introducing a gene for encoding citric acid synthase from Eskerikia Coli. 
On the one hand, molybdenum is an essential transition element functioning as an important role in the biological world, which is required in enzymes catalyzing a diversity of essential reaction in the metabolism of carbon, sulfur and nitrogen. However, since molybdenum itself does not have biological activity, it should be formed a complex with pterin mixture in cell to have proper activity, which is called a molybdenum cofactor. Because a path of a molybdenum cofactor biosynthesis is evolutionally well preserved, many proteins and its gene participating in the path have high homogeny from bacteria to a higher animal comprising human being.
In a biosynthesis process of molybdenum cofactor, guanosine triphosphate converts into molybdopterine precursor Z and then it converts into molybdopterine, and lastly molybdenum combines to them.
The molybdenum cofactor biosynthesis enzyme A which is involved in the first step in the process of molybdenum cofactor biosynthesis, has a role together with molybdenum cofactor biosynthesis enzyme C in converting guanosine triphosphate into molybdopterine precursor Z.
Some of more than 50 species of enzymes which is known by containing molybdenum cofactor in bacteria, participate in the core reaction of nitrogen metabolism procedure. For example, nitrate reductase acts as a major enzyme which is catalyzed a metabolism of inorganic nitrogen source via the reaction of reducing nitrate to nitrite. Moreover, in the production of L-lysine having two nitrogen atoms per a molecular, the nitrogen metabolism can be very important.
Based on the above fact, we kept on trying to increase an activity of enzymes involved in nitrogen metabolism by intensifying the biosynthesis of molybdenum cofactor, through which it can be made smooth supply of nitrogen atom to enhance production efficacy of L-lysine such that the present invention was contrived.